title: Purification, crystallization and preliminary X-ray crystallographic analysis of the transport unit of the monomeric autotransporter AIDA-I from Escherichia coli.
abstract: The adhesin involved in diffuse adherence (AIDA-I) from Escherichia coli belongs to the group of autotransporters, specifically the type Va secretion system (T5aSS). All autotransporter systems contain a C-terminal β-domain, which forms a barrel-like structure in the outer membrane with a hydrophilic pore allowing passenger translocation across the outer membrane. The passenger domain harbours the biological activity in the extracellular space and functions, for example, as an adhesin, an enzyme and a toxin. The exact transport mechanism of passenger translocation across the outer membrane is not clear at present. Thus, structure determination of the transport unit of AIDA-I could provide new insights into the transport mechanism. Here, the purification, crystallization and preliminary X-ray crystallographic studies of the transport unit of AIDA-I are reported.
authors.affiliation: Institute of Biochemistry, Heinrich-Heine-Universität, Düsseldorf, Germany.
authors.forename: Iris
authors.initials: I
authors.lastname: Gawarzewski
authors.forename: Britta
authors.initials: B
authors.lastname: Tschapek
authors.forename: Astrid
authors.initials: A
authors.lastname: Hoeppner
authors.forename: Joachim
authors.initials: J
authors.lastname: Jose
authors.forename: Sander H J
authors.initials: SH
authors.lastname: Smits
authors.forename: Lutz
authors.initials: L
authors.lastname: Schmitt
mesh_terms: D018830:Adhesins, Escherichia coli / Q000737:chemistry* / Q000302:isolation & purification*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D011489:Protein Denaturation; D021381:Protein Transport
chemical_list: C075559:AIDA-I protein, E coli; D018830:Adhesins, Escherichia coli
keywords: Escherichia coli; transport unit of AIDA-I